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B Venkataram V Prasad - One of the best experts on this subject based on the ideXlab platform.

  • Cell Attachment protein vp8 of a human rotavirus specifically interacts with a type histo blood group antigen
    Nature, 2012
    Co-Authors: Liya Hu, Rita Czako, Mary K. Estes, Sue E Crawford, Nicolas W Cortespenfield, David F Smith, Jacques Le Pendu, B Venkataram V Prasad
    Abstract:

    This crystallographic study shows the Attachment of human rotavirus VP8* to histo blood group A antigen, and suggests how changes within the structure of VP8* could allow switching from sialylated to non-sialylated glycan receptor. Rotaviruses are the major pathogens of infantile gastroenteritis. They attach to the surfaces of Cells through interactions with specific Cellular glycans. Animal rotaviruses bind to glycans with terminal sialic acid, whereas human rotavirus strains are sialidase insensitive. Venkataram Prasad and colleagues now show that certain human rotavirus strains bind to and infect Cells through A-type histo-blood group antigen (HBGA), suggesting that susceptibility to specific human rotavirus strains might be influenced by different blood-group antigens, a phenomenon reported in Helicobacter pylori and norovirus infection. Crystallographic studies show how HBGA binds to the Attachment protein of human norovirus (VP8), and suggest how subtle changes in the structure of VP8 might allow receptor switching. As with many other viruses, the initial Cell Attachment of rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific Cellular glycans1,2,3,4. The distally located VP8* domain of the rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that ‘sialidase-sensitive’ animal rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas ‘sialidase-insensitive’ human rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies1,3,6,7, it is not yet known how VP8* of human rotaviruses interacts with Sia and whether their Cell Attachment necessarily involves sialoglycans. Here we show that VP8* of a human rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 Cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary Cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial Cell Attachment of human rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood Cells8, and are recognized as susceptibility and Cell Attachment factors for gastric pathogens like Helicobacter pylori9 and noroviruses10. Our crystallographic studies show that the A-type HBGA binds to the human rotavirus VP8* at the same location as the Sia in the VP8* of animal rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific human rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world’s population.

  • Cell Attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen
    Nature, 2012
    Co-Authors: Sue E Crawford, Rita Czako, Mary K. Estes, David F Smith, Jacques Le Pendu, Nicolas W. Cortes-penfield, B Venkataram V Prasad
    Abstract:

    As with many other viruses, the initial Cell Attachment of rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific Cellular glycans. The distally located VP8* domain of the rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that 'sialidase-sensitive' animal rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas 'sialidase-insensitive' human rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies, it is not yet known how VP8* of human rotaviruses interacts with Sia and whether their Cell Attachment necessarily involves sialoglycans. Here we show that VP8* of a human rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 Cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary Cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial Cell Attachment of human rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood Cells, and are recognized as susceptibility and Cell Attachment factors for gastric pathogens like Helicobacter pylori and noroviruses. Our crystallographic studies show that the A-type HBGA binds to the human rotavirus VP8* at the same location as the Sia in the VP8* of animal rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific human rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world's population.

Sue E Crawford - One of the best experts on this subject based on the ideXlab platform.

  • Cell Attachment protein vp8 of a human rotavirus specifically interacts with a type histo blood group antigen
    Nature, 2012
    Co-Authors: Liya Hu, Rita Czako, Mary K. Estes, Sue E Crawford, Nicolas W Cortespenfield, David F Smith, Jacques Le Pendu, B Venkataram V Prasad
    Abstract:

    This crystallographic study shows the Attachment of human rotavirus VP8* to histo blood group A antigen, and suggests how changes within the structure of VP8* could allow switching from sialylated to non-sialylated glycan receptor. Rotaviruses are the major pathogens of infantile gastroenteritis. They attach to the surfaces of Cells through interactions with specific Cellular glycans. Animal rotaviruses bind to glycans with terminal sialic acid, whereas human rotavirus strains are sialidase insensitive. Venkataram Prasad and colleagues now show that certain human rotavirus strains bind to and infect Cells through A-type histo-blood group antigen (HBGA), suggesting that susceptibility to specific human rotavirus strains might be influenced by different blood-group antigens, a phenomenon reported in Helicobacter pylori and norovirus infection. Crystallographic studies show how HBGA binds to the Attachment protein of human norovirus (VP8), and suggest how subtle changes in the structure of VP8 might allow receptor switching. As with many other viruses, the initial Cell Attachment of rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific Cellular glycans1,2,3,4. The distally located VP8* domain of the rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that ‘sialidase-sensitive’ animal rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas ‘sialidase-insensitive’ human rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies1,3,6,7, it is not yet known how VP8* of human rotaviruses interacts with Sia and whether their Cell Attachment necessarily involves sialoglycans. Here we show that VP8* of a human rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 Cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary Cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial Cell Attachment of human rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood Cells8, and are recognized as susceptibility and Cell Attachment factors for gastric pathogens like Helicobacter pylori9 and noroviruses10. Our crystallographic studies show that the A-type HBGA binds to the human rotavirus VP8* at the same location as the Sia in the VP8* of animal rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific human rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world’s population.

  • Cell Attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen
    Nature, 2012
    Co-Authors: Sue E Crawford, Rita Czako, Mary K. Estes, David F Smith, Jacques Le Pendu, Nicolas W. Cortes-penfield, B Venkataram V Prasad
    Abstract:

    As with many other viruses, the initial Cell Attachment of rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific Cellular glycans. The distally located VP8* domain of the rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that 'sialidase-sensitive' animal rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas 'sialidase-insensitive' human rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies, it is not yet known how VP8* of human rotaviruses interacts with Sia and whether their Cell Attachment necessarily involves sialoglycans. Here we show that VP8* of a human rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 Cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary Cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial Cell Attachment of human rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood Cells, and are recognized as susceptibility and Cell Attachment factors for gastric pathogens like Helicobacter pylori and noroviruses. Our crystallographic studies show that the A-type HBGA binds to the human rotavirus VP8* at the same location as the Sia in the VP8* of animal rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific human rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world's population.

Peter X - One of the best experts on this subject based on the ideXlab platform.

  • nano fibrous scaffolding architecture selectively enhances protein adsorption contributing to Cell Attachment
    Journal of Biomedical Materials Research Part A, 2003
    Co-Authors: Kyung Mi Woo, Victor J Chen, Peter X
    Abstract:

    Tissue engineering aims at resolving problems such as donor shortage and immune rejection faced by transplantation. Scaffolds (artificial extraCellular matrices) have critical roles in tissue engineering. Recently, we developed nano-fibrous poly(L-lactic acid) scaffolds under the hypothesis that synthetic nano-fibrous scaffolding, mimicking the structure of natural collagen fibers, could create a more favorable microenvironment for Cells. This is the first report that the nano-fibrous architecture built in three-dimensional scaffolds improved the features of protein adsorption, which mediates Cell interactions with scaffolds. Scaffolds with nano-fibrous pore walls adsorbed four times more serum proteins than scaffolds with solid pore walls. More interestingly, the nano-fibrous architecture selectively enhanced protein adsorption including fibronectin and vitronectin, even though both scaffolds were made from the same poly(L-lactic acid) material. Furthermore, nano-fibrous scaffolds also allowed >1.7 times of osteoblastic Cell Attachment than scaffolds with solid pore walls. These results demonstrate that the biomimetic nano-fibrous architecture serves as superior scaffolding for tissue engineering.

  • nano fibrous scaffolding architecture enhances protein adsorption and Cell Attachment
    MRS Proceedings, 2002
    Co-Authors: Kyung Mi Woo, Victor J Chen, Peter X
    Abstract:

    Tissue engineering aims at resolving problems such as donor shortage and immune rejection faced in transplantation. Scaffolds (artificial extraCellular matrices) play critical roles in tissue engineering. Recently, we developed nano-fibrous poly(L-lactic acid) (PLLA) scaffolds under the hypothesis that synthetic nano-fibrous scaffolding, mimicking the structure of natural collagen fibers, could create a more favorable microenvironment for Cells. This is the first report that the nano-fibrous architecture built in three-dimensional scaffolds improved the features of protein adsorption, which mediates Cell interactions with scaffolds. Scaffolds with nano-fibrous pore walls adsorbed 4 times more serum proteins than scaffolds with solid pore walls. More interestingly, the nano-fibrous architecture selectively enhanced protein adsorption including fibronectin and vitronectin, even though both scaffolds were made from the same PLLA material. Furthermore, nano-fibrous scaffolds also allowed more than 1.7 times of osteoblastic Cell Attachment than scaffolds with “solid” pore walls. These results demonstrate that the biomimetic nano-fibrous architecture serves as superior scaffolding for tissue engineering.

David F Smith - One of the best experts on this subject based on the ideXlab platform.

  • Cell Attachment protein vp8 of a human rotavirus specifically interacts with a type histo blood group antigen
    Nature, 2012
    Co-Authors: Liya Hu, Rita Czako, Mary K. Estes, Sue E Crawford, Nicolas W Cortespenfield, David F Smith, Jacques Le Pendu, B Venkataram V Prasad
    Abstract:

    This crystallographic study shows the Attachment of human rotavirus VP8* to histo blood group A antigen, and suggests how changes within the structure of VP8* could allow switching from sialylated to non-sialylated glycan receptor. Rotaviruses are the major pathogens of infantile gastroenteritis. They attach to the surfaces of Cells through interactions with specific Cellular glycans. Animal rotaviruses bind to glycans with terminal sialic acid, whereas human rotavirus strains are sialidase insensitive. Venkataram Prasad and colleagues now show that certain human rotavirus strains bind to and infect Cells through A-type histo-blood group antigen (HBGA), suggesting that susceptibility to specific human rotavirus strains might be influenced by different blood-group antigens, a phenomenon reported in Helicobacter pylori and norovirus infection. Crystallographic studies show how HBGA binds to the Attachment protein of human norovirus (VP8), and suggest how subtle changes in the structure of VP8 might allow receptor switching. As with many other viruses, the initial Cell Attachment of rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific Cellular glycans1,2,3,4. The distally located VP8* domain of the rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that ‘sialidase-sensitive’ animal rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas ‘sialidase-insensitive’ human rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies1,3,6,7, it is not yet known how VP8* of human rotaviruses interacts with Sia and whether their Cell Attachment necessarily involves sialoglycans. Here we show that VP8* of a human rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 Cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary Cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial Cell Attachment of human rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood Cells8, and are recognized as susceptibility and Cell Attachment factors for gastric pathogens like Helicobacter pylori9 and noroviruses10. Our crystallographic studies show that the A-type HBGA binds to the human rotavirus VP8* at the same location as the Sia in the VP8* of animal rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific human rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world’s population.

  • Cell Attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen
    Nature, 2012
    Co-Authors: Sue E Crawford, Rita Czako, Mary K. Estes, David F Smith, Jacques Le Pendu, Nicolas W. Cortes-penfield, B Venkataram V Prasad
    Abstract:

    As with many other viruses, the initial Cell Attachment of rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific Cellular glycans. The distally located VP8* domain of the rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that 'sialidase-sensitive' animal rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas 'sialidase-insensitive' human rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies, it is not yet known how VP8* of human rotaviruses interacts with Sia and whether their Cell Attachment necessarily involves sialoglycans. Here we show that VP8* of a human rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 Cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary Cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial Cell Attachment of human rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood Cells, and are recognized as susceptibility and Cell Attachment factors for gastric pathogens like Helicobacter pylori and noroviruses. Our crystallographic studies show that the A-type HBGA binds to the human rotavirus VP8* at the same location as the Sia in the VP8* of animal rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific human rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world's population.

Rita Czako - One of the best experts on this subject based on the ideXlab platform.

  • Cell Attachment protein vp8 of a human rotavirus specifically interacts with a type histo blood group antigen
    Nature, 2012
    Co-Authors: Liya Hu, Rita Czako, Mary K. Estes, Sue E Crawford, Nicolas W Cortespenfield, David F Smith, Jacques Le Pendu, B Venkataram V Prasad
    Abstract:

    This crystallographic study shows the Attachment of human rotavirus VP8* to histo blood group A antigen, and suggests how changes within the structure of VP8* could allow switching from sialylated to non-sialylated glycan receptor. Rotaviruses are the major pathogens of infantile gastroenteritis. They attach to the surfaces of Cells through interactions with specific Cellular glycans. Animal rotaviruses bind to glycans with terminal sialic acid, whereas human rotavirus strains are sialidase insensitive. Venkataram Prasad and colleagues now show that certain human rotavirus strains bind to and infect Cells through A-type histo-blood group antigen (HBGA), suggesting that susceptibility to specific human rotavirus strains might be influenced by different blood-group antigens, a phenomenon reported in Helicobacter pylori and norovirus infection. Crystallographic studies show how HBGA binds to the Attachment protein of human norovirus (VP8), and suggest how subtle changes in the structure of VP8 might allow receptor switching. As with many other viruses, the initial Cell Attachment of rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific Cellular glycans1,2,3,4. The distally located VP8* domain of the rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that ‘sialidase-sensitive’ animal rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas ‘sialidase-insensitive’ human rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies1,3,6,7, it is not yet known how VP8* of human rotaviruses interacts with Sia and whether their Cell Attachment necessarily involves sialoglycans. Here we show that VP8* of a human rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 Cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary Cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial Cell Attachment of human rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood Cells8, and are recognized as susceptibility and Cell Attachment factors for gastric pathogens like Helicobacter pylori9 and noroviruses10. Our crystallographic studies show that the A-type HBGA binds to the human rotavirus VP8* at the same location as the Sia in the VP8* of animal rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific human rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world’s population.

  • Cell Attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen
    Nature, 2012
    Co-Authors: Sue E Crawford, Rita Czako, Mary K. Estes, David F Smith, Jacques Le Pendu, Nicolas W. Cortes-penfield, B Venkataram V Prasad
    Abstract:

    As with many other viruses, the initial Cell Attachment of rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific Cellular glycans. The distally located VP8* domain of the rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that 'sialidase-sensitive' animal rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas 'sialidase-insensitive' human rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies, it is not yet known how VP8* of human rotaviruses interacts with Sia and whether their Cell Attachment necessarily involves sialoglycans. Here we show that VP8* of a human rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 Cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary Cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial Cell Attachment of human rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood Cells, and are recognized as susceptibility and Cell Attachment factors for gastric pathogens like Helicobacter pylori and noroviruses. Our crystallographic studies show that the A-type HBGA binds to the human rotavirus VP8* at the same location as the Sia in the VP8* of animal rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific human rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world's population.